ID A0A1A2AYG0_9MYCO Unreviewed; 699 AA.
AC A0A1A2AYG0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN ORFNames=A5753_18480 {ECO:0000313|EMBL:OBF61227.1};
OS Mycobacterium sp. 852002-51971_SCH5477799-a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834106 {ECO:0000313|EMBL:OBF61227.1, ECO:0000313|Proteomes:UP000091887};
RN [1] {ECO:0000313|EMBL:OBF61227.1, ECO:0000313|Proteomes:UP000091887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852002-51971_SCH5477799-a {ECO:0000313|EMBL:OBF61227.1,
RC ECO:0000313|Proteomes:UP000091887};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027,
CC ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBF61227.1}.
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DR EMBL; LZIF01000118; OBF61227.1; -; Genomic_DNA.
DR RefSeq; WP_067132806.1; NZ_LZIF01000118.1.
DR AlphaFoldDB; A0A1A2AYG0; -.
DR STRING; 1834106.A5753_18480; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000091887; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 375..557
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 699 AA; 75324 MW; 4718EAA01FBAB243 CRC64;
MTTLEEISTL TQPHLPDDWT ELDSAAVDTI RVLAADAVQK VGNGHPGTAM SLAPLAYTLF
QRAMRHDPSD THWLGRDRFV LSCGHSSLTL YLQLYLGGFG LELSDIESLR TWGSKTPGHP
EFRHTKGVEI TTGPLGQGLA SAVGMAMAAR YERGLFDPDA APGTSPFDHF IYAIASDGDI
EEGVTSEASS LAAVQQLGNL IVFYDHNEIS IEDDTNIALC EDTAARYRAY GWHVQEVEGG
ENVVAIEEAI ANAKAATDRP SFISLRTIIG YPAPKLMNTG KAHGAALGDE EVAAVKEILG
FDPDKKFEVR DEVIAHTRKL VDRGKEAHEK WQADFDAWAE GQPERKALLD RLTAEELPDG
WDDDLPHWDP GSDPIATRKA SNEVLNAVGP KLPELWGGSA DLAGSNNTTI KGADSFGPPS
ISTKDYTAHW YGRTLHFGVR EHAMGAILSG IVLHGPTRAY GGTFLQFSDY MRPAVRLASL
MDIDTIYVWT HDSVGLGEDG PTHQPIEHLA ALRAIPNLSV VRPADANETA YAWRTVLARG
NGSGPVGLML TRQNVPVLEG TSADGVARGG YILGSDGEEA GQDPDVVLIA TGSEVQLAVG
AQKLLADKDI VARVVSMPCV EWFESQPDDY RDSVLPPTVS ARVAVEAGVA QSWHKLVGDT
GKIVSIEHYG ESADYETIFR EFGFTAEAVA AAAEEVVDN
//
